Radical–radical reactions of superoxide: A potential route to toxicity
Abstract
Superoxide reacts with many radicals, such as phenoxyl radicals, at near diffusion-controlled rates. These reactions are usually considered to be repair processes and have received little biological attention. However, addition of superoxide to give hydroperoxides and secondary oxidation products can also occur. The relative contributions of addition and repair vary depending on the properties of the phenol. With tyrosine, addition to give tyrosine hydroperoxide predominates, but in peptides the efficiency of hydroperoxide formation depends on the proximity of free amine groups. Radicals from other phenolic compounds, such as alpha-tocopherol and serotonin, also undergo addition reactions with superoxide. Physiologically, these reactions are likely to be more significant than dimerization when both radicals are generated together. They warrant attention as potential contributors to superoxide toxicity.
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The tyrosine hydroperoxide can be formed in the ortho or para position relative to the phenoxyl radical due to resonant forms of Tyr.
“The hydroperoxide, due to the resonant forms of Tyr, can be formed in the ortho or para position with respect to the phenoxyl radical [138,139,140], Figure 51 and Figure 52.”
From Superoxide Anion Chemistry—Its Role at the Core of the Innate Immunity (2023) · cites this paper as [138]
Cites
Free radicals in biology and medicine
Gutteridge, J. M. C. (1991) · General Pharmacology The Vascular System · doi:10.1016/0306-3623(91)90478-o · Cited by 17,178 · see citing works
McCord, J. M., & Fridovich, I. (1969) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)63504-5 · Cited by 12,952 · see citing works
Beckman, J. S., Beckman, T. W., Chen, J., Marshall, P. A., & Freeman, B. A. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.4.1620 · Cited by 7,029 · see citing works
Nitric oxide, superoxide, and peroxynitrite: the good, the bad, and ugly
Beckman, J. S., & Koppenol, W. H. (1996) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.1996.271.5.c1424 · Cited by 5,513 · see citing works
Free Radicals in Biology and Medicine
Land, E. J. (1990) · International Journal of Radiation Biology · doi:10.1080/09553009014552071 · Cited by 4,871 · see citing works
The reaction of NO with superoxide
Huie, R. E., & Padmaja, S. (1993) · Free Radical Research Communications · doi:10.3109/10715769309145868 · Cited by 2,121 · see citing works
Biochemistry and pathology of radical-mediated protein oxidation
Dean, R. T., Fu, S., Stocker, R., & Davies, M. J. (1997) · Biochemical Journal · doi:10.1042/bj3240001 · Cited by 1,678 · see citing works
Brzezinski, A. (1997) · New England Journal of Medicine · doi:10.1056/nejm199701163360306 · Cited by 1,549 · see citing works
Rubbo, H., Radí, R., Trujillo, M., Telleri, R., Kalyanaraman, B., Barnes, S., KIRK, M. C., & Freeman, B. Α. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)47160-8 · Cited by 1,350 · see citing works
Myeloperoxidase: a key regulator of neutrophil oxidant production
Kettle, A. J., & Winterbourn, C. C. (1997) · Redox Report · doi:10.1080/13510002.1997.11747085 · Cited by 660 · see citing works
Self-citationPeroxynitrite‐mediated oxidative protein modifications
Ischiropoulos, H., & Al‐Mehdi, A. B. (1995) · FEBS Letters · doi:10.1016/0014-5793(95)00307-u · Cited by 610 · see citing works
Denicola, A., Freeman, B. A., Trujillo, M., & Radi, R. (1996) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1996.0363 · Cited by 593 · see citing works
Photo-oxidation of proteins and its role in cataractogenesis
Davies, M. J., & Truscott, R. J. W. (2001) · Journal of Photochemistry and Photobiology B Biology · doi:10.1016/s1011-1344(01)00208-1 · Cited by 446 · see citing works
Superoxide as an intracellular radical sink
Winterbourn, C. C. (1993) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(93)90512-s · Cited by 365 · see citing works
Self-citationTyrosyl radical generated by myeloperoxidase catalyzes the oxidative cross-linking of proteins.
Heinecke, J. W., Li, W., Francis, G. A., & Goldstein, J. A. (1993) · Journal of Clinical Investigation · doi:10.1172/jci116531 · Cited by 354 · see citing works
The basic chemistry of nitrogen monoxide and peroxynitrite
Koppenol, W. H. (1998) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(98)00093-8 · Cited by 338 · see citing works
Formation of peroxides in amino acids and proteins exposed to oxygen free radicals
Gebicki, S., & Gebicki, J. M. (1993) · Biochemical Journal · doi:10.1042/bj2890743 · Cited by 305 · see citing works
Mechanism of carbon dioxide-catalyzed oxidation of tyrosine by peroxynitrite
Lymar, S. V., Jiang, Q., & Hurst, J. K. (1996) · Biochemistry · doi:10.1021/bi960331h · Cited by 299 · see citing works
Nitric Oxide Regulation of Superoxide and Peroxynitrite-dependent Lipid Peroxidation
KIRK, M. C., & Freeman, B. Α. (1994) · Cited by 272 · see citing works
O'Brien, P. J. (2000) · Chemico-Biological Interactions · doi:10.1016/s0009-2797(00)00201-5 · Cited by 259 · see citing works
Evidence for roles of radicals in protein oxidation in advanced human atherosclerotic plaque
Fu, S., Davies, M. J., Stocker, R., & Dean, R. T. (1998) · Biochemical Journal · doi:10.1042/bj3330519 · Cited by 256 · see citing works
Formation of dityrosine cross-links in proteins by oxidation of tyrosine residues
Aeschbach, R., Amadoò, R., & Neukom, H. (1976) · Biochimica et Biophysica Acta (BBA) - Protein Structure · doi:10.1016/0005-2795(76)90064-7 · Cited by 256 · see citing works
O’Donnell, V. B., Chumley, P. H., Hogg, N., Bloodsworth, A., Darley-Usmar, V. M., & Freeman, B. Α. (1997) · Biochemistry · doi:10.1021/bi971891z · Cited by 253 · see citing works
Kinetics of Oxidation of Tyrosine and Dityrosine by Myeloperoxidase Compounds I and II
Marquez‐Curtis, L. A., & Dunford, H. B. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.51.30434 · Cited by 237 · see citing works
Reactions of Hindered Phenols. II. Base-Catalyzed Oxidations of Hindered Phenols*
Kharasch, M. S., & Joshi, B. S. (1957) · The Journal of Organic Chemistry · doi:10.1021/jo01362a034 · Cited by 230 · see citing works
Superoxide and iron: Partners in crime
Liochev, S. I., & Fridovich, I. (1999) · International Union of Biochemistry and Molecular Biology: Life · doi:10.1080/152165499307161 · Cited by 219 · see citing works
Wright, A., Bubb, W. A., Hawkins, C. L., & Davies, M. J. (2002) · Photochemistry and Photobiology · doi:10.1562/0031-8655(2002)0760035sompoe2.0.co2 · Cited by 202 · see citing works
Klinger, M. H. F. (1997) · Anatomy and Embryology · doi:10.1007/s004290050075 · Cited by 201 · see citing works
Tew, D. G., & de Montellano, P. R. O. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)77915-0 · Cited by 181 · see citing works
Tyrosine Nitration by Simultaneous Generation of ⋅NO and O⨪2 under Physiological Conditions
Goldstein, S., Czapski, G., Lind, J., & Merényi, G. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.5.3031 · Cited by 177 · see citing works
O'Brien, P. J. (1988) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(88)90025-1 · Cited by 166 · see citing works
The effect of oxygen, antioxidants, and superoxide radical on tyrosine phenoxyl radical dimerization
Hunter, E. P. L., Desrosiers, M. F., & Simic, M. G. (1989) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(89)90064-6 · Cited by 153 · see citing works
Nitric oxide rapidly scavenges tyrosine and tryptophan radicals
Eiserich, J. P., Butler, J., van der Vliet, A., Cross, C. E., & Halliwell, B. B. (1995) · Biochemical Journal · doi:10.1042/bj3100745 · Cited by 151 · see citing works
Jacob, J. S., Cistola, D. P., Hsu, F., Muzaffar, S., Mueller, D. M., Hazen, S. L., & Heinecke, J. W. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.33.19950 · Cited by 150 · see citing works
Galati, G., Chan, T. S., Wu, B., & O'Brien, P. J. (1999) · Chemical Research in Toxicology · doi:10.1021/tx980271b · Cited by 148 · see citing works
Jin, F., Leitich, J., & von Sonntag, C. (1993) · Journal of the Chemical Society Perkin Transactions 2 · doi:10.1039/p29930001583 · Cited by 146 · see citing works
Crosslinking of DNA and proteins induced by protein hydroperoxides
Gebicki, S., & Gebicki, J. M. (1999) · Biochemical Journal · doi:10.1042/bj3380629 · Cited by 127 · see citing works
Kinetic behavior and thermochemical properties of phenoxy radicals
Mahoney, L. R., & DaRooge, M. A. (1975) · Journal of the American Chemical Society · doi:10.1021/ja00849a039 · Cited by 124 · see citing works
Free radical combination reactions involving phenoxyl radicals
Jönsson, M., Lind, J., Reitberger, T., Eriksen, T. E., & Merényi, G. (1993) · The Journal of Physical Chemistry · doi:10.1021/j100133a018 · Cited by 117 · see citing works
Heinecke, J. W. (2002) · Toxicology · doi:10.1016/s0300-483x(02)00192-0 · Cited by 116 · see citing works
SIMINIAK, T., Flores, N. A., & Sheridan, D. J. (1995) · European Heart Journal · doi:10.1093/oxfordjournals.eurheartj.a060880 · Cited by 111 · see citing works
Phenol Coupling Initiated by One-electron Oxidation of Tyrosine Units in Peptides and Histone
Prütz, W. A., Butler, J., & Land, E. J. (1983) · International Journal of Radiation Biology and Related Studies in Physics Chemistry and Medicine · doi:10.1080/09553008314550981 · Cited by 110 · see citing works
Eosinophil peroxidase produces hypobromous acid in the airways of stable asthmatics
Aldridge, R. E., Chan, T., van Dalen, C. J., Senthilmohan, R., WINN, M. C., Venge, P., Town, G. I., & Kettle, A. J. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)00976-0 · Cited by 109 · see citing works
Self-citationOxidation of serotonin by superoxide radical: Implications to neurodegenerative brain disorders
Wrona, M. Z., & Dryhurst, G. (1998) · Chemical Research in Toxicology · doi:10.1021/tx970185w · Cited by 105 · see citing works
Giulivi, C., & Davies, K. J. A. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m010697200 · Cited by 104 · see citing works
Zhang, R., Shen, Z., Nauseef, W. M., & Hazen, S. L. (2002) · Blood · doi:10.1182/blood.v99.5.1802.h8001802_1802_1810 · Cited by 95 · see citing works
Detection and reactions of the globin radical in haemoglobin
McArthur, K. M., & Davies, M. J. (1993) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/0167-4838(93)90002-9 · Cited by 91 · see citing works
Morgan, P. E., Dean, R. T., & Davies, M. J. (2002) · European Journal of Biochemistry · doi:10.1046/j.1432-1033.2002.02845.x · Cited by 89 · see citing works
Biological fate of amino acid, peptide and protein hydroperoxides
Fu, S., Gebicki, S., Jessup, W., Gebicki, J. M., & Dean, R. T. (1995) · Biochemical Journal · doi:10.1042/bj3110821 · Cited by 88 · see citing works
Leeuwenburgh, C., Hansen, P. A., Holloszy, J. O., & Heinecke, J. W. (1999) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.1999.276.1.r128 · Cited by 87 · see citing works
Myeloperoxidase-catalyzed oxidation of melatonin by activated neutrophils
de Oliveira Silva, S., Ximenes, V. F., Catalani, L. H., & Campa, A. (2000) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2000.3993 · Cited by 72 · see citing works
Myeloperoxidase-Dependent Generation of a Tyrosine Peroxide by Neutrophils
Winterbourn, C. C., Pichorner, H., & Kettle, A. J. (1997) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1996.9773 · Cited by 71 · see citing works
Self-citationTaylor, D. R., Sears, M. R., & Cockcroft, D. W. (1996) · Medical Clinics of North America · doi:10.1016/s0025-7125(05)70465-x · Cited by 70 · see citing works
Pichorner, H., Metodiewa, D., & Winterbourn, C. C. (1995) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1995.0064 · Cited by 70 · see citing works
Self-citationInactivation of cellular caspases by peptide‐derived tryptophan and tyrosine peroxides
Hampton, M. B., Morgan, P. E., & Davies, M. J. (2002) · FEBS Letters · doi:10.1016/s0014-5793(02)03240-4 · Cited by 61 · see citing works
Reaction of superoxide with phenoxyl-type radicals
d’Alessandro, N., Bianchi, G., Fang, X., Jin, F., Schuchmann, H., & von Sonntag, C. (2000) · Journal of the Chemical Society Perkin Transactions 2 · doi:10.1039/b003346o · Cited by 59 · see citing works
Bhattacharjee, S., Pennathur, S., Byun, J., Crowley, J. R., Mueller, D. M., Gischler, J., Hotchkiss, R. S., & Heinecke, J. W. (2001) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.2001.2557 · Cited by 55 · see citing works
Bedard, L. L., Young, M. J., Hall, D., Paul, T., & Ingold, K. U. (2001) · Journal of the American Chemical Society · doi:10.1021/ja011076d · Cited by 52 · see citing works
Pulse radiolysis study on the reactivity of Trolox C phenoxyl radical with superoxide anion
Cadenas, E., Merényi, G., & Lind, J. U. (1989) · FEBS Letters · doi:10.1016/0014-5793(89)80966-4 · Cited by 52 · see citing works
Fang, X., Jin, F., Jin, H., & Sonntag, C. V. (1998) · Journal of the Chemical Society, Perkin Transactions 2 · doi:10.1039/a706979k · Cited by 51 · see citing works
Characterization of a Tyrosyl Radical in Prostaglandin Endoperoxide Synthase-2
Hsi, L. C., Hoganson, C. W., Babcock, Ǵ., & Smith, W. L. (1994) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1994.2114 · Cited by 46 · see citing works
Induction of DNA damage by oxidised amino acids and proteins
Luxford, C., Dean, R. T., & Davies, M. J. (2002) · Biogerontology · doi:10.1023/a:1015228001561 · Cited by 43 · see citing works
Tyrosine Iminoxyl Radical Formation from Tyrosyl Radical/Nitric Oxide and Nitrosotyrosine
Sturgeon, B. E., Glover, R. E., Chen, Y., Burka, L. T., & Mason, R. P. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m106835200 · Cited by 40 · see citing works
Kettle, A. J., Carr, A. C., & Winterbourn, C. C. (1994) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(94)90111-2 · Cited by 39 · see citing works
Self-citationGaudu, P., Nivière, V., Pétillot, Y., Kauppi, B., & Fontecave, M. (1996) · FEBS Letters · doi:10.1016/0014-5793(96)00480-2 · Cited by 37 · see citing works
Production and identification of bityrosine in horseradish peroxidase-H2O2-tyrosine system
Ushijima, Y., Nakano, M., & Goto, T. (1984) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(84)91370-6 · Cited by 33 · see citing works
Jiang, X., Wrona, M. Z., & Dryhurst, G. (1999) · Chemical Research in Toxicology · doi:10.1021/tx9801615 · Cited by 32 · see citing works
Effectiveness of phenol antioxidants and the properties of quinolide peroxides
Roginskii, V. A., Dubinskii, V. Z., Shlyapnikova, I. A., & Miller, V. B. (1977) · European Polymer Journal · doi:10.1016/0014-3057(77)90178-1 · Cited by 29 · see citing works
Effects of β2-agonists on airway tone and bronchial responsiveness
Larj, M. J., & Bleecker, E. R. (2002) · Journal of Allergy and Clinical Immunology · doi:10.1067/mai.2002.130045 · Cited by 28 · see citing works
Shima, N., Stolz, D. B., Miyazaki, M., Gohda, E., Higashio, K., & Michalopoulos, G. K. (1998) · Journal of Cellular Physiology · doi:10.1002/(sici)1097-4652(199810)177:1 · Cited by 26 · see citing works
Submolecular adventures of brain tyrosine: what are we searching for now?
Kochman, A., Kośka, C., & Metodiewa, D. (2002) · Amino Acids · doi:10.1007/s00726-001-0114-6 · Cited by 24 · see citing works
Landolfi, R., & Cristofaro, R. D. (2000) · Thrombosis and Haemostasis · doi:10.1055/s-0037-1613796 · Cited by 24 · see citing works
Ziment, I. (1995) · CHEST Journal · doi:10.1378/chest.107.5_supplement.198s · Cited by 23 · see citing works
Drug derived radicals: mediators of the side effects of anti-inflammatory drugs?
Halliwell, B. B., Evans, P., Kaur, H., & Chirico, S. (1992) · Annals of the Rheumatic Diseases · doi:10.1136/ard.51.11.1261 · Cited by 19 · see citing works
Nitric oxide: a radical molecule in quest of free radicals in proteins
Guittet, O., Roy, B., & Lepoivre, M. (1999) · Cellular and Molecular Life Sciences · doi:10.1007/s000180050356 · Cited by 19 · see citing works
ChemInform Abstract: THE KINETIC BEHAVIOR AND THERMOCHEMICAL PROPERTIES OF PHENOXY RADICALS
Mahoney, L. R., & DaRooge, M. A. (1975) · ChemInform · doi:10.1002/chin.197542077 · Cited by 6 · see citing works
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Heger, M., van Golen, R. F., Broekgaarden, M., & Michel, M. C. (2013) · Pharmacological Reviews · doi:10.1124/pr.110.004044 · Cited by 581 · see citing works
Protein Tyrosine Nitration: Biochemical Mechanisms and Structural Basis of Functional Effects
Radi, R. (2013) · Accounts of Chemical Research · doi:10.1021/ar300234c · Cited by 525 · see citing works
Redox Reactions and Microbial Killing in the Neutrophil Phagosome
Winterbourn, C. C., & Kettle, A. J. (2013) · Antioxidants & Redox Signaling · doi:10.1089/ars.2012.4827 · Cited by 468 · see citing works
Self-citationMüller, F. L., Song, W., Liu, Y., Chaudhuri, A. R., Pieke-Dahl, S., Strong, R., Huang, T., Epstein, C. J., Roberts, L. J., CSETE, M. E., et al. (2006) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2006.01.036 · Cited by 447 · see citing works
Photodynamic Therapy: Current Status and Future Directions
Benov, L. (2014) · Medical Principles and Practice · doi:10.1159/000362416 · Cited by 428 · see citing works
Winterbourn, C. C. (2013) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2013.05.004 · Cited by 420 · see citing works
Self-citationCadet, J., Douki, T., & Ravanat, J. (2015) · Photochemistry and Photobiology · doi:10.1111/php.12368 · Cited by 355 · see citing works
Superoxide Anion Chemistry—Its Role at the Core of the Innate Immunity
Andrés, C. M. C., Pérez de la Lastra, J. M., Andrés Juan, C., Plou, F. J., & Pérez-Lebeña, E. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24031841 · Cited by 342 · see citing works
Free radicals and polyphenols: The redox chemistry of neurodegenerative diseases
Losada‐Barreiro, S., & Bravo‐Díaz, C. (2017) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2017.03.061 · Cited by 295 · see citing works
Fotiou, T., Triantis, T. M., Kaloudis, T., Ο'Shea, K. Ε., Dionysiou, D. D., & Hiskia, A. E. (2015) · Water Research · doi:10.1016/j.watres.2015.12.006 · Cited by 219 · see citing works
Evaluation of antioxidant activity of Cassia siamea flowers
Kaur, G., Alam, M. S., Jabbar, Z., Javed, K., & Athar, M. (2006) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2006.05.021 · Cited by 196 · see citing works
Antioxidative nanomaterials and biomedical applications
Liu, Y., & Shi, J. (2019) · Nano Today · doi:10.1016/j.nantod.2019.05.008 · Cited by 173 · see citing works
Ceruloplasmin Is an Endogenous Inhibitor of Myeloperoxidase
Chapman, A., Mocatta, T. J., Shiva, S., Seidel, A., Chen, B., Khalilova, I. S., Paumann-Page, M., Jameson, G. N. L., Winterbourn, C. C., & Kettle, A. J. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.418970 · Cited by 153 · see citing works
Self-citationCadet, J., Loft, S. H., Oliński, R., Evans, M. D., Białkowski, K., Wagner, J. R., Dedon, P. C., Möller, P., Greenberg, M. M., & Cooke, M. S. (2012) · Free Radical Research · doi:10.3109/10715762.2012.659248 · Cited by 143 · see citing works
Superoxide Converts Indigo Carmine to Isatin Sulfonic Acid
Kettle, A. J., Clark, B. M., & Winterbourn, C. C. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m400334200 · Cited by 142 · see citing works
Self-citationPeroxidase Substrate Nanosensors for MR Imaging
Pérez, J. M. S., Simeone, F. J., Tsourkas, A., Josephson, L., & Weissleder, R. (2003) · Nano Letters · doi:10.1021/nl034983k · Cited by 135 · see citing works
Urate as a Physiological Substrate for Myeloperoxidase
Meotti, F. C., Jameson, G. N. L., Turner, R., Harwood, D. T., Stockwell, S., Rees, M. D., Thomas, S. R., & Kettle, A. J. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.172460 · Cited by 133 · see citing works
Self-citationFloriano-Sánchez, E., Floriano-Sánchez, E., Villanueva, C., Floriano-Sánchez, E., Villanueva, C., Medina‐Campos, O. N., Floriano-Sánchez, E., Villanueva, C., Medina‐Campos, O. N., Rocha-Mendoza, D., et al. (2006) · Free Radical Research · doi:10.1080/10715760500419365 · Cited by 130 · see citing works
Houée-Lévin, C., Bobrowski, K., Horakova, L., Karademir, B., Schöneich, C., Davies, M. J., & Spickett, C. M. (2015) · Free Radical Research · doi:10.3109/10715762.2015.1007968 · Cited by 126 · see citing works
Catalysis of Peroxide Reduction by Fast Reacting Protein Thiols
Zeida, A., Trujillo, M., Ferrer‐Sueta, G., Denicola, A., Estrin, D. A., & Radí, R. (2019) · Chemical Reviews · doi:10.1021/acs.chemrev.9b00371 · Cited by 114 · see citing works
Requirements for superoxide-dependent tyrosine hydroperoxide formation in peptides
WINTERBOURN, C. C., PARSONS-MAIR, H. N., GEBICKI, S., GEBICKI, J. M., & DAVIES, M. J. (2004) · Biochemical Journal · doi:10.1042/bj20040259 · Cited by 112 · see citing works
Self-citationPospı́šil, P., Prasad, A., & Rác, M. (2019) · Biomolecules · doi:10.3390/biom9070258 · Cited by 114 · see citing works
Novel Biomarkers of Heart Failure
Savic-Radojevic, A. R., Pljesa-Ercegovac, M. S., Matic, M., Simic, D., Radovanović, S., & Simic, T. P. (2016) · Advances in clinical chemistry · doi:10.1016/bs.acc.2016.09.002 · Cited by 110 · see citing works
Gouthamchandra, K., Mahmood, R., & Manjunatha, H. (2010) · Environmental Toxicology and Pharmacology · doi:10.1016/j.etap.2010.03.005 · Cited by 105 · see citing works
Zielonka, J., Zhao, H., Xu, Y., & Kalyanaraman, B. (2005) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2005.05.001 · Cited by 99 · see citing works
Mechanisms underlying degradation pathways of microcystin-LR with doped TiO2 photocatalysis
Hu, X., Hu, X., Tang, C., Wen, S., Wu, X., Long, J., Xiong, Y., Wang, H., & Zhou, L. (2017) · Chemical Engineering Journal · doi:10.1016/j.cej.2017.07.161 · Cited by 91 · see citing works
Biological chemistry of superoxide radicals
Winterbourn, C. C. (2020) · ChemTexts · doi:10.1007/s40828-019-0101-8 · Cited by 91 · see citing works
Self-citationBai, W. K., Zhang, F. J., He, T., Su, P. W., Ying, X., Zhang, L. L., & Wang, T. Z. (2016) · PLoS ONE · doi:10.1371/journal.pone.0167339 · Cited by 81 · see citing works
Medina‐Campos, O. N., Barrera, D., Segoviano‐Murillo, S., Rocha-Mendoza, D., Maldonado, P. D., Mendoza-Patiño, N., & Pedraza‐Chaverrí, J. (2007) · Food and Chemical Toxicology · doi:10.1016/j.fct.2007.05.002 · Cited by 77 · see citing works
Baik, J. S., Kim, S.-S., Lee, J.-A., Oh, T., Kim, J.-Y., Lee, N. H., & Hyun, C. (2008) · PubMed · Cited by 74 · see citing works
Light-driven breakdown of microcystin-LR in water: A critical review
Xie, G., Hu, X., Du, Y., Jin, Q., Liu, Y., Tang, C., Hu, X., Li, G., Chen, Z., Zhou, D., et al. (2021) · Chemical Engineering Journal · doi:10.1016/j.cej.2021.129244 · Cited by 73 · see citing works
Zhang, Y., & Blough, N. V. (2016) · Environmental Science & Technology · doi:10.1021/acs.est.6b02919 · Cited by 73 · see citing works
Gurgul-Convey, E., Mehmeti, I., Lortz, S., & Lenzen, S. (2011) · Journal of Molecular Medicine · doi:10.1007/s00109-011-0747-1 · Cited by 70 · see citing works
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Cabello, M. C., Chen, G., Melville, M. J., Osman, R., Kumar, G., Domaille, D. W., & Lippert, A. R. (2024) · Chemical Reviews · doi:10.1021/acs.chemrev.3c00892 · Cited by 67 · see citing works
Antioxidant activity of wild edible plants in the Black Sea Region of Turkey
Özen, T. (2009) · Grasas y Aceites · doi:10.3989/gya.075509 · Cited by 67 · see citing works
Kim, S. S., Baik, J. S., Oh, T., Yoon, W., Lee, N. H., & Hyun, C. (2008) · Bioscience Biotechnology and Biochemistry · doi:10.1271/bbb.70388 · Cited by 67 · see citing works
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Millington, K. R. (2006) · Coloration Technology · doi:10.1111/j.1478-4408.2006.00045.x · Cited by 66 · see citing works
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Freewan, M., Rees, M. D., Plaza, T. S. S., Glaros, E. N., Lim, Y. J., Wang, X., Yeung, A. W. S., Witting, P. K., Terentis, A. C., & Thomas, S. R. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.410993 · Cited by 66 · see citing works
Peskin, A. V., & Winterbourn, C. C. (2003) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(03)00502-1 · Cited by 59 · see citing works
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Scheeline, A., & Behrens, R. L. (2012) · Biophysical Chemistry · doi:10.1016/j.bpc.2012.03.008 · Cited by 58 · see citing works
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Self-citationCarroll, L., Pattison, D. I., Davies, J. B., Anderson, R. F., Lopez-Alarcon, C., & Davies, M. J. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.02.033 · Cited by 48 · see citing works
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Kujbida, P. D. S., Hatanaka, E., Čampa, A., Colepicolo, P., & Pinto, E. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.12.177 · Cited by 44 · see citing works
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Seidel, A., Parker, H. A., Turner, R., Dickerhof, N., Khalilova, I. S., Wilbanks, S. M., Kettle, A. J., & Jameson, G. N. L. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.544957 · Cited by 41 · see citing works
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Kettle, A. J., Ashby, L. V., Winterbourn, C. C., & Dickerhof, N. (2023) · Immunological Reviews · doi:10.1111/imr.13183 · Cited by 40 · see citing works
Self-citationDwinandha, D., Zhang, B., & Fujii, M. (2021) · Chemosphere · doi:10.1016/j.chemosphere.2021.132763 · Cited by 39 · see citing works
Cano-Europa, E., López-Galindo, G. E., Hernández-Garcı́a, A., Blas-Valdivia, V., Casas, C. Á. G., Vargas-Lascari, M., & Ortiz-Butrón, R. (2008) · Life Sciences · doi:10.1016/j.lfs.2008.09.005 · Cited by 37 · see citing works
Bushira, F. A., Wang, P., Hussain, A., Li, H., & Jin, Y. (2023) · ACS Applied Nano Materials · doi:10.1021/acsanm.3c00243 · Cited by 35 · see citing works
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Mukherjee, S., Seal, M., & Dey, S. G. (2014) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-014-1193-7 · Cited by 35 · see citing works
Roux, D. M. L., Powers, L. C., & Blough, N. V. (2021) · Environmental Science & Technology · doi:10.1021/acs.est.1c04043 · Cited by 35 · see citing works
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Arslan, B. A., Ertan, N. Z., Kuruca, S. E., & Karakaş, Z. (2006) · Pediatric Hematology and Oncology · doi:10.1080/08880010500506420 · Cited by 34 · see citing works
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Self-citationDavies, M. J. (2012) · Wiley eBooks · doi:10.1002/9781119953678.rad045 · Cited by 34 · see citing works
Das, A. B., Nauser, T., Koppenol, W. H., Kettle, A. J., Winterbourn, C. C., & Nagy, P. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.02.006 · Cited by 33 · see citing works
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Kaur, G., Lone, I. A., Athar, M., & Alam, M. S. (2006) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2006.10.012 · Cited by 29 · see citing works
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Alam, M. S., Kaur, G., Jabbar, Z., Javed, K., & Athar, M. (2006) · Phytotherapy Research · doi:10.1002/ptr.1882 · Cited by 28 · see citing works
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Self-citationLone, I. A., Kaur, G., Athar, M., & Alam, M. S. (2007) · Food and Chemical Toxicology · doi:10.1016/j.fct.2007.03.021 · Cited by 24 · see citing works
Aravind, P., & Prasad, M. N. V. (2005) · Plant Science · doi:10.1016/j.plantsci.2005.03.028 · Cited by 22 · see citing works
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Suh, K. S., Choi, E. M., Rhee, S. Y., Oh, S., Kim, S. W., Pak, Y. K., Choe, W., Ha, J., & Chon, S. (2017) · Journal of Environmental Science and Health Part A · doi:10.1080/10934529.2017.1294964 · Cited by 21 · see citing works
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Miwa, S., Müller, F. L., & Beckman, K. B. (2008) · Humana Press eBooks · doi:10.1007/978-1-59745-420-9_2 · Cited by 20 · see citing works
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Abid, R., Mahmood, R., Rajesh, K. P.-G., & Swamy, B. E. K. (2014) · International Journal of Pharmacy and Pharmaceutical Sciences · Cited by 15 · see citing works
Tran, P. L., Kopel, J. J., Ristić, B., Marsh, H. D., Fralick, J. A., & Reid, T. W. (2022) · Advances in Redox Research · doi:10.1016/j.arres.2022.100031 · Cited by 14 · see citing works
Rattmann, Y. D., Méndez‐Sánchez, S. C., Furian, A. F., Paludo, K. S., de Souza, L. M., Dartora, N., Oliveira, M. S., Costa, E. M. D. S., Miguel, O. G., Sassaki, G. L., et al. (2010) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2010.11.030 · Cited by 13 · see citing works
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Li, H., Zang, J., Xia, X., Wang, Z., Wang, L., El-Seedi, H. R., Xu, X., Zhao, G., & Du, M. (2023) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2023.04.013 · Cited by 10 · see citing works
Cho, E.-K., Gal, S.-W., & Choi, Y. (2010) · Journal of Applied Biological Chemistry · doi:10.3839/jabc.2010.017 · Cited by 10 · see citing works
Field, S. M., & Villamena, F. A. (2008) · Chemical Research in Toxicology · doi:10.1021/tx8001687 · Cited by 10 · see citing works
Kuppusamy, U. R., & Tan, J. (2011) · PubMed · Cited by 10 · see citing works
Rahate, K., Rajasekaran, A., & Arulkumaran, K. S. G. (2012) · Cited by 10 · see citing works
Özen, T., & Demirtaş, İ. (2015) · Journal of Essential Oil Bearing Plants · doi:10.1080/0972060x.2014.998719 · Cited by 9 · see citing works
Barros, M. P., Araujo-Chaves, J. C., Brito, A. M. M., & Nantes, I. L. (2020) · Chemical Research in Toxicology · doi:10.1021/acs.chemrestox.0c00122 · Cited by 9 · see citing works
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Kuriakose, S. V., & Prasad, M. N. V. (2008) · Wiley eBooks · doi:10.1002/9780470370124.ch16 · Cited by 9 · see citing works
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Schempp, H., Vogel, S., Hückelhoven, R., & Heilmann, J. (2010) · Free Radical Research · doi:10.3109/10715762.2010.515216 · Cited by 7 · see citing works
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Kettle, A. J., & Winterbourn, C. C. (2015) · Royal Society of Chemistry eBooks · doi:10.1039/9781782622628-00272 · Cited by 7 · see citing works
Self-citationTHE FREE RADICAL-SCAVENGING PROPERTY OF CHONDROITIN SULFATE FROM PIG LARYNGEAL CARTILAGE IN VITRO
Xiong, S., & Jin, Z. (2007) · Journal of Food Biochemistry · doi:10.1111/j.1745-4514.2007.00096.x · Cited by 7 · see citing works
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Winterbourn, C. C. (2026) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2026.04.003 · Cited by 6 · see citing works
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Roux, D. M. L., Powers, L. C., & Blough, N. V. (2023) · Environmental Science & Technology · doi:10.1021/acs.est.3c08254 · Cited by 6 · see citing works
Dinuclear Zn Complex: Phenoxyl Radical Formation Driven by Superoxide Coordination
Squarcina, A., Fehn, D., Senft, L., Langer, J., & Ivanović‐Burmazović, I. (2021) · Zeitschrift für anorganische und allgemeine Chemie · doi:10.1002/zaac.202000468 · Cited by 6 · see citing works
Estimation of Oxidative Stress Involvement by Superoxide Dismutase Variation in Cardiac Arrhythmias.
Bezna, M., Cârstea, D., Bezna, M., Pisoschi, C. G., Istrătoaie, O., Alexandru, D. O., Efrem, I. C., & Melinte, R. (2017) · Europe PMC (PubMed Central) · doi:10.12865/chsj.43.02.03 · Cited by 6 · see citing works
Osmotic and Oxidative stress in hepatic encephalopathy
Schliess, F., Görg, B., Reinehr, R., Bidmon, H. J., & Häussinger, D. (2007) · Springer eBooks · doi:10.1007/1-4020-4456-9_2 · Cited by 6 · see citing works
Muñoz‐Rugeles, L., Galano, A., & Alvarez-Idaboy, J. R. (2020) · New Journal of Chemistry · doi:10.1039/c9nj04998c · Cited by 5 · see citing works
Regulation of the Redox Environment
Cano-Europa, E., Blas-Valdivia, V., Franco-Colín, M., & Ortiz-Butrón, R. (2015) · InTech eBooks · doi:10.5772/61515 · Cited by 5 · see citing works
Ho, J., Kang, E.-R., Yoon, H., Jeon, H., Jun, W., WATSON, R. R., & Lee, J. (2011) · Bioscience Biotechnology and Biochemistry · doi:10.1271/bbb.100840 · Cited by 5 · see citing works
- Authors
- Winterbourn, C. C., & Kettle, A. J.
- Corresponding author
- Winterbourn, Christine C.
- Venue
- Biochemical and Biophysical Research Communications
- Publisher
- Elsevier BV
- Published
- 2003-06
- Volume
- 305
- Issue
- 3
- Pages
- 729-736
- ISSN
- 0006-291X (ISSN-L)
- OpenAlex
- W1967305386
- Cited by
- 118
- References
- 76
- Citations by year
- 2026: 3 · 2025: 2 · 2024: 2 · 2023: 6 · 2022: 2 · 2021: 7 · 2020: 3 · 2019: 3 · 2018: 2 · 2017: 4 · 2016: 3 · 2015: 6 · 2014: 10 · 2013: 4 · 2012: 8
- FWCI
- 4.92
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Biochemical and Biophysical Research Communications (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Health Research Council of New Zealand
- Topics
- Physical Sciences › Chemistry › Organic Chemistry › Free Radicals and Antioxidants
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Health Sciences › Medicine › Biochemistry › Antioxidant Activity and Oxidative Stress
- Keywords
- superoxide, phenoxyl radicals, radical-radical reactions, hydroperoxide formation, phenol oxidation, alpha-tocopherol, serotonin, radical dimerization, diffusion-controlled reaction
- MeSH terms
- Animals, Free Radicals, Indoles, Models, Chemical, Nitric Oxide, Peptides, Peroxides, Phenols, Proteins, Superoxides, Tyrosine, Vitamin E
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